L-Tyrosine (BioDeep_00000000157)

 

Secondary id: BioDeep_00000229645, BioDeep_00000398091

natural product human metabolite PANOMIX_OTCML-2023 Endogenous blood metabolite BioNovoGene_Lab2019 Volatile Flavor Compounds


代谢物信息卡片


(2S)-2-amino-3-(4-hydroxyphenyl)propanoic acid

化学式: C9H11NO3 (181.0738896)
中文名称: L-酪氨酸, 酪氨酸
谱图信息: 最多检出来源 Homo sapiens(blood) 0.02%

Reviewed

Last reviewed on 2024-07-01.

Cite this Page

L-Tyrosine. BioDeep Database v3. PANOMIX ltd, a top metabolomics service provider from China. https://query.biodeep.cn/s/l-tyrosine (retrieved 2024-11-21) (BioDeep RN: BioDeep_00000000157). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).

分子结构信息

SMILES: C1=CC(=CC=C1CC(C(=O)O)N)O
InChI: InChI=1S/C9H11NO3/c10-8(9(12)13)5-6-1-3-7(11)4-2-6/h1-4,8,11H,5,10H2,(H,12,13)

描述信息

Tyrosine (Tyr) or L-tyrosine is an alpha-amino acid. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon). Amino acids are organic compounds that contain amino (–NH2) and carboxyl (–COOH) functional groups, along with a side chain (R group) specific to each amino acid. L-tyrosine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Tyrosine is found in all organisms ranging from bacteria to plants to animals. It is classified as a non-polar, uncharged (at physiological pH) aromatic amino acid. Tyrosine is a non-essential amino acid, meaning the body can synthesize it – usually from phenylalanine. The conversion of phenylalanine to tyrosine is catalyzed by the enzyme phenylalanine hydroxylase, a monooxygenase. This enzyme catalyzes the reaction causing the addition of a hydroxyl group to the end of the 6-carbon aromatic ring of phenylalanine, such that it becomes tyrosine. Tyrosine is found in many high-protein food products such as chicken, turkey, fish, milk, yogurt, cottage cheese, cheese, peanuts, almonds, pumpkin seeds, sesame seeds, soy products, lima beans, avocados and bananas. Tyrosine is one of the few amino acids that readily passes the blood-brain barrier. Once in the brain, it is a precursor for the neurotransmitters dopamine, norepinephrine and epinephrine, better known as adrenalin. These neurotransmitters are an important part of the bodys sympathetic nervous system, and their concentrations in the body and brain are directly dependent upon dietary tyrosine. Tyrosine is not found in large concentrations throughout the body, probably because it is rapidly metabolized. Folic acid, copper and vitamin C are cofactor nutrients of these reactions. Tyrosine is also the precursor for hormones, including thyroid hormones (diiodotyrosine), catecholestrogens and the major human pigment, melanin. Tyrosine is an important amino acid in many proteins, peptides and even enkephalins, the bodys natural pain reliever. Valine and other branched amino acids, and possibly tryptophan and phenylalanine may reduce tyrosine absorption. A number of genetic errors of tyrosine metabolism have been identified, such as hawkinsinuria and tyrosinemia I. The most common feature of these diseases is the increased amount of tyrosine in the blood, which is marked by decreased motor activity, lethargy and poor feeding. Infection and intellectual deficits may occur. Vitamin C supplements can help reverse these disease symptoms. Some adults also develop elevated tyrosine in their blood. This typically indicates a need for more vitamin C. More tyrosine is needed under stress, and tyrosine supplements prevent the stress-induced depletion of norepinephrine and can help aleviate biochemical depression. However, tyrosine may not be good for treating psychosis. Many antipsychotic medications apparently function by inhibiting tyrosine metabolism. L-Dopa, which is directly used in Parkinsons, is made from tyrosine. Tyrosine, the nutrient, can be used as an adjunct in the treatment of Parkinsons. Peripheral metabolism of tyrosine necessitates large doses of tyrosine, however, compared to L-Dopa (http://www.dcnutrition.com). In addition to its role as a precursor for neurotransmitters, tyrosine plays an important role for the function of many proteins. Within many proteins or enzymes, certain tyrosine residues can be tagged (at the hydroxyl group) with a phosphate group (phosphorylated) by specialized protein kinases. In its phosphorylated form, tyrosine is called phosphotyrosine. Tyrosine phosphorylation is considered to be one of the key steps in signal transduction and regulation of enzymatic activity. Tyrosine (or its precursor phenylalanine) is also needed to synthesize the benzoquinone structure which forms part of coenzyme Q10.
L-tyrosine is an optically active form of tyrosine having L-configuration. It has a role as an EC 1.3.1.43 (arogenate dehydrogenase) inhibitor, a nutraceutical, a micronutrient and a fundamental metabolite. It is an erythrose 4-phosphate/phosphoenolpyruvate family amino acid, a proteinogenic amino acid, a tyrosine and a L-alpha-amino acid. It is functionally related to a L-tyrosinal. It is a conjugate base of a L-tyrosinium. It is a conjugate acid of a L-tyrosinate(1-). It is an enantiomer of a D-tyrosine. It is a tautomer of a L-tyrosine zwitterion.
Tyrosine is a non-essential amino acid. In animals it is synthesized from [phenylalanine]. It is also the precursor of [epinephrine], thyroid hormones, and melanin.
L-Tyrosine is a metabolite found in or produced by Escherichia coli (strain K12, MG1655).
L-Tyrosine is the levorotatory isomer of the aromatic amino acid tyrosine. L-tyrosine is a naturally occurring tyrosine and is synthesized in vivo from L-phenylalanine. It is considered a non-essential amino acid; however, in patients with phenylketonuria who lack phenylalanine hydroxylase and cannot convert phenylalanine into tyrosine, it is considered an essential nutrient. In vivo, tyrosine plays a role in protein synthesis and serves as a precursor for the synthesis of catecholamines, thyroxine, and melanin.
Tyrosine is an essential amino acid that readily passes the blood-brain barrier. Once in the brain, it is a precursor for the neurotransmitters dopamine, norepinephrine and epinephrine, better known as adrenalin. These neurotransmitters are an important part of the bodys sympathetic nervous system, and their concentrations in the body and brain are directly dependent upon dietary tyrosine. Tyrosine is not found in large concentrations throughout the body, probably because it is rapidly metabolized. Folic acid, copper and vitamin C are cofactor nutrients of these reactions. Tyrosine is also the precursor for hormones, thyroid, catecholestrogens and the major human pigment, melanin. Tyrosine is an important amino acid in many proteins, peptides and even enkephalins, the bodys natural pain reliever. Valine and other branched amino acids, and possibly tryptophan and phenylalanine may reduce tyrosine absorption. A number of genetic errors of tyrosine metabolism occur. Most common is the increased amount of tyrosine in the blood of premature infants, which is marked by decreased motor activity, lethargy and poor feeding. Infection and intellectual deficits may occur. Vitamin C supplements reverse the disease. Some adults also develop elevated tyrosine in their blood. This indicates a need for more vitamin C. More tyrosine is needed under stress, and tyrosine supplements prevent the stress-induced depletion of norepinephrine and can cure biochemical depression. However, tyrosine may not be good for psychosis. Many antipsychotic medications apparently function by inhibiting tyrosine metabolism. L-dopa, which is directly used in Parkinsons, is made from tyrosine. Tyrosine, the nutrient, can be used as an adjunct in the treatment of Parkinsons. Peripheral metabolism of tyrosine necessitates large doses of tyrosine, however, compared to L-dopa.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
Dietary supplement, nutrient. Flavouring ingredient. L-Tyrosine is found in many foods, some of which are blue crab, sweet rowanberry, lemon sole, and alpine sweetvetch.
An optically active form of tyrosine having L-configuration.

L-Tyrosine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=60-18-4 (retrieved 2024-07-01) (CAS RN: 60-18-4). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).
L-Tyrosine is a non-essential amino acid which can inhibit citrate synthase activity in the posterior cortex.
L-Tyrosine is a non-essential amino acid which can inhibit citrate synthase activity in the posterior cortex.

同义名列表

132 个代谢物同义名

L-Tyrosine, from non-animal source, meets EP, USP testing specifications, suitable for cell culture, >=99.0\\%; Benzeneethanaminium,a-carboxy-4-hydroxy-N,N,N-trimethyl-,inner salt,(as)-; Melanin synthesized from Tyr substrate catalyzed by tyrosinase for 6 hrs; 2-amino-3-(4-hydroxyphen yl)-2-amino-3-(4-hydroxyphenyl)-Propanoic acid; 2-amino-3-(4-hydroxyphen yl)-2-amino-3-(4-hydroxyphenyl)-Propanoate; L-Tyrosine, United States Pharmacopeia (USP) Reference Standard; Tyrosine, European Pharmacopoeia (EP) Reference Standard; L-Tyrosine, certified reference material, TraceCERT(R); Benzenepropanoic acid, .alpha.-amino-4-hydroxy-, (S)-; .alpha.-Amino-.beta.-(4-hydroxyphenyl)propionic acid; Benzenepropanoic acid, alpha-amino-4-hydroxy-, (S)-; Propanoic acid, 2-amino-3-(4-hydroxyphenyl)-, (S)-; alpha-Amino-4-hydroxybenzenepropanoic acid, (S)-; (S)-.alpha.-Amino-4-hydroxybenzenepropanoic acid; alpha-Amino-beta-(4-hydroxyphenyl)propionic acid; Propanoic acid, 2-amino-3-(4-hydroxyphenyl)-(S)-; 2-Amino-3-(4-hydroxyphenyl)propanoic acid, (S)-; (S)-alpha-amino-4-hydroxy-Benzenepropanoic acid; 2-Amino-3-(4-hydroxyphenyl)propanoic acid-(S)-; (S)-alpha-Amino-4-hydroxybenzenepropanoic acid; (2S)-2-amino-3-(4-hydroxyphenyl)propanoic acid; (-)-.alpha.-Amino-p-hydroxyhydrocinnamic acid; L-Tyrosine, Cell Culture Reagent (H-L-Tyr-OH); LEVODOPA IMPURITY, L-TYROSINE- [USP IMPURITY]; (S)-2-Amino-3-(p-hydroxyphenyl)propionic acid; (S)-2-Amino-3-(4-hydroxyphenyl)propanoic acid; alpha-Amino-p-hydroxyhydrocinnamic acid, (-)-; (2S)-2-amino-3-(4-hydroxyphenyl)propanoicacid; (S)-2-Amino-3-(4-hydroxyphenyl)propionic acid; (S)-alpha-amino-4-hydroxy-Benzenepropanoate; (-)-alpha-Amino-p-hydroxyhydrocinnamic acid; (S)-a-amino-4-hydroxy-Benzenepropanoic acid; L-Tyrosine, Vetec(TM) reagent grade, >=98\\%; (S)-alpha-Amino-4-hydroxybenzenepropanoate; (S)-Α-amino-4-hydroxybenzenepropanoic acid; (S)-a-Amino-4-hydroxybenzenepropanoic acid; (2S)-2-Amino-3-(4-hydroxyphenyl)propanoate; L-2-Amino-3-p-hydroxyphenylpropanoic acid; (S)-2-Amino-3-(p-hydroxyphenyl)propionate; N-ACETYLTYROSINE IMPURITY A [EP IMPURITY]; L-Tyrosine, reagent grade, >=98\\% (HPLC); (-)-a-Amino-p-hydroxyhydrocinnamic acid; (S)-a-amino-4-hydroxy-Benzenepropanoate; (-)-Α-amino-p-hydroxyhydrocinnamic acid; L-Tyrosine, SAJ special grade, >=99.0\\%; (-)-alpha-Amino-p-hydroxyhydrocinnamate; (S)-a-Amino-4-hydroxybenzenepropanoate; (S)-Α-amino-4-hydroxybenzenepropanoate; L-Tyrosine, Free Base - CAS 60-18-4; (-)-Α-amino-p-hydroxyhydrocinnamate; (-)-a-Amino-p-hydroxyhydrocinnamate; L-Tyrosine, BioUltra, >=99.0\\% (NT); DIETHYL1,3,5-BENZENETRICARBOXYLATE; LEVODOPA IMPURITY B [EP IMPURITY]; (S)-3-(4-HYDROXYPHENYL)ALANINE; Levodopa impurity, l-tyrosine-; (S)-3-(p-Hydroxyphenyl)alanine; beta-(p-Hydroxyphenyl)alanine; L-Tyrosine, Vetec(TM), 98.5\\%; 3-(4-Hydroxyphenyl)-L-alanine; IS_4-HYDROXYPHENYL-D4-ALANINE; L-Tyrosine non-animal source; L-Phenylalanine, 4-hydroxy-; L-Phenylalanine-4-hydroxy-; 4-Hydroxy-L-phenylalanine; TYROSINE [USP MONOGRAPH]; TYROSINE [EP MONOGRAPH]; L-Tyrosine, >=97\\%, FG; TYROSINE [ORANGE BOOK]; Tyrosine (L-Tyrosine); Benzenepropanoic acid; L-Tyrosine, monomer; L-TYROSINE [USP-RS]; Tyrosine [USAN:INN]; Tirosina [Spanish]; Tyrosine (USP/INN); Tyrosine, L-isomer; Tyrosine, L- (8CI); Tyrosine, L isomer; Tyrosinum [Latin]; L-Tyrosine (JP17); TYROSINE [WHO-DD]; L-TYROSINE [FHFI]; Benzenepropanoate; TYROSINE [VANDF]; L-TYROSINE [FCC]; L-TYROSINE [JAN]; L-Tyrosine (9CI); (S)-(-)-Tyrosine; TYROSINE [MART.]; plovamer-acetate; TYROSINE [INCI]; UNII-42HK56048U; TYROSINE [HSDB]; TYROSINE [USAN]; Tox21_111594_1; L-(-)-Tyrosine; Tyrosine (VAN); L-Tyrosine,(S); TYROSINE [INN]; TYROSINE [II]; para-Tyrosine; TYROSINE [MI]; para Tyrosine; (-) tyrosine; L-p-Tyrosine; Tyrosine, L-; L-[U-14C]Tyr; (L)-Tyrosine; Tox21_111594; (S)-Tyrosine; CAS-60-18-4; L Tyrosine; 42HK56048U; L-Tyrosine; p-Tyrosine; Tyrosinum; AI3-09055; -tyrosine; L-Tyrosin; L-TYR-OH; Tyrosine; H-Tyr-OH; tirosina; L-Tyr; H-Tyr; 2csm; tyr; Y; Tyrosine; L-Tyrosine; Tyrosine



数据库引用编号

68 个数据库交叉引用编号

分类词条

相关代谢途径

Reactome(0)

BioCyc(2)

PlantCyc(0)

代谢反应

75 个相关的代谢反应过程信息。

Reactome(0)

BioCyc(5)

WikiPathways(9)

Plant Reactome(0)

INOH(2)

PlantCyc(0)

COVID-19 Disease Map(0)

PathBank(59)

PharmGKB(0)

488 个相关的物种来源信息

在这里通过桑基图来展示出与当前的这个代谢物在我们的BioDeep知识库中具有相关联信息的其他代谢物。在这里进行关联的信息来源主要有：

  • PubMed: 来源于PubMed文献库中的文献信息，我们通过自然语言数据挖掘得到的在同一篇文献中被同时提及的相关代谢物列表，这个列表按照代谢物同时出现的文献数量降序排序，取前10个代谢物作为相关研究中关联性很高的代谢物集合展示在桑基图中。
  • NCBI Taxonomy: 通过文献数据挖掘，得到的代谢物物种来源信息关联。这个关联信息同样按照出现的次数降序排序，取前10个代谢物作为高关联度的代谢物集合展示在桑吉图上。
  • Chemical Taxonomy: 在物质分类上处于同一个分类集合中的其他代谢物
  • Chemical Reaction: 在化学反应过程中，存在为当前代谢物相关联的生化反应过程中的反应底物或者反应产物的关联代谢物信息。

点击图上的相关代谢物的名称，可以跳转到相关代谢物的信息页面。



文献列表

  • Kimberly N Karin, Mohammed A Mustafa, Justin L Poklis, Belle Buzzi, Joel E Schlosburg, Linda Parker, M Imad Damaj, Aron H Lichtman. N-oleoyl alanine attenuates nicotine reward and spontaneous nicotine withdrawal in mice. Drug and alcohol dependence. 2024 Jun; 259(?):111276. doi: 10.1016/j.drugalcdep.2024.111276. [PMID: 38676968]
  • Srihari Shankar, Ti Weng Chew, Vishnu Priyanka Reddy Chichili, Boon Chuan Low, J Sivaraman. Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP. Cellular and molecular life sciences : CMLS. 2024 May; 81(1):216. doi: 10.1007/s00018-024-05238-8. [PMID: 38740643]
  • Hao Huang, Ying Wei, Shaojun Huang, Shijian Lu, Huasheng Su, Liuhui Ma, Weiping Huang. Integrated metabolomic and transcriptomic analyses provide insights into regulation mechanisms during bulbous stem development in the Chinese medicinal herb plant, Stephania kwangsiensis. BMC plant biology. 2024 Apr; 24(1):276. doi: 10.1186/s12870-024-04956-2. [PMID: 38605285]
  • Álvaro Pérez-Valero, Juan Serna-Diestro, Albert Tafur Rangel, Simona Barbuto Ferraiuolo, Chiara Schiraldi, Eduard J Kerkhoven, Claudio J Villar, Felipe Lombó. Biosynthesis of Hesperetin, Homoeriodictyol, and Homohesperetin in a Transcriptomics-Driven Engineered Strain of Streptomyces albidoflavus. International journal of molecular sciences. 2024 Apr; 25(7):. doi: 10.3390/ijms25074053. [PMID: 38612864]
  • Mette G B Pedersen, Nikolaj Rittig, Maj Bangshaab, Kristoffer Berg-Hansen, Nigopan Gopalasingam, Lars C Gormsen, Esben Søndergaard, Niels Møller. Effects of exogenous lactate on lipid, protein, and glucose metabolism-a randomized crossover trial in healthy males. American journal of physiology. Endocrinology and metabolism. 2024 Apr; 326(4):E443-E453. doi: 10.1152/ajpendo.00301.2023. [PMID: 38324259]
  • Chun Chu, Shengquan Liu, Liangui Nie, Hongming Hu, Yi Liu, Jun Yang. The interactions and biological pathways among metabolomics products of patients with coronary heart disease. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie. 2024 Apr; 173(?):116305. doi: 10.1016/j.biopha.2024.116305. [PMID: 38422653]
  • Alex H Crum, Lisa Philander, Lucas Busta, Ya Yang. Traditional medicinal use is linked with apparency, not specialized metabolite profiles in the order Caryophyllales. American journal of botany. 2024 Apr; 111(4):e16308. doi: 10.1002/ajb2.16308. [PMID: 38581167]
  • I-Tsu Chyuan, Hsiu-Jung Liao, Tse-Hua Tan, Huai-Chia Chuang, Yu-Chuan Chu, Meng-Hsun Pan, Chien-Sheng Wu, Ching-Liang Chu, Bor-Ching Sheu, Ping-Ning Hsu. Association of TRAIL receptor with phosphatase SHP-1 enables repressing T cell receptor signaling and T cell activation through inactivating Lck. Journal of biomedical science. 2024 Mar; 31(1):33. doi: 10.1186/s12929-024-01023-8. [PMID: 38532423]
  • Tim Schäfer, Fabian Haun, Markus Gressler, Peter Spiteller, Dirk Hoffmeister. Parallel Evolution of Asco- and Basidiomycete O-Prenyltransferases. Journal of natural products. 2024 Mar; 87(3):576-582. doi: 10.1021/acs.jnatprod.3c01120. [PMID: 38231181]
  • Kateryna Kukil, Pia Lindberg. Metabolic engineering of Synechocystis sp. PCC 6803 for the improved production of phenylpropanoids. Microbial cell factories. 2024 Feb; 23(1):57. doi: 10.1186/s12934-024-02330-3. [PMID: 38369470]
  • Abhijith G Karkisaval, Rowan Hassan, Andrew Nguyen, Benjamin Balster, Faisal Abedin, Ratnesh Lal, Suren A Tatulian. The structure of tyrosine-10 favors ionic conductance of Alzheimer's disease-associated full-length amyloid-β channels. Nature communications. 2024 Feb; 15(1):1296. doi: 10.1038/s41467-023-43821-y. [PMID: 38351257]
  • Nishanthika Thenmozhi Kulasekaran, Mary Leema Thilakam, Dharani Gopal, Jung-Kul Lee, Jeya Marimuthu. Denovo production of resveratrol by engineered Saccharomyces cerevisiae W303-1a using pretreated Gracilaria corticata extracts. Biotechnology letters. 2024 Feb; 46(1):19-28. doi: 10.1007/s10529-023-03441-4. [PMID: 37987932]
  • Mohammed Bouhadi, Oussama Abchir, Imane Yamari, Amal El Hamsas El Youbi, Anas Azgaoui, Samir Chtita, Houda El Hajjouji, M'hammed El Kouali, Mohammed Talbi, Hassan Fougrach. Genotoxic effects and mitosis aberrations of chromium (VI) on root cells of Vicia faba and its molecular docking analysis. Plant physiology and biochemistry : PPB. 2024 Feb; 207(?):108361. doi: 10.1016/j.plaphy.2024.108361. [PMID: 38237423]
  • Jingjing Shi, Jiawei Zhang, Dan Sun, Leifei Zhao, Yao Chi, Caiqiu Gao, Yucheng Wang, Chao Wang. Protein profile analysis of tension wood development in response to artificial bending and gravitational stimuli in Betula platyphylla. Plant science : an international journal of experimental plant biology. 2024 Feb; 339(?):111957. doi: 10.1016/j.plantsci.2023.111957. [PMID: 38122834]
  • Xiaoxia Wang, Chenping Kang, Wanqian Guo, Lilan Yuan, Haoran Zhang, Qiong Zhang, Qianqian Xiao, Weidong Hao. Chlormequat chloride induced activation of calmodulin mediated PI3K/AKT signaling pathway led to impaired sperm quality in pubertal mice. Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association. 2024 Jan; 185(?):114475. doi: 10.1016/j.fct.2024.114475. [PMID: 38286265]
  • Anna Szuba-Trznadel, Anna Jama-Rodzeńska, Bernard Gałka, Rafał Ramut, Zygmunt Król, Daniel Jarki, Dragana Latković. The impact of the distribution method for struvite (Crystal Green) on the chemical composition of soybean and their utility in animal nutrition. Scientific reports. 2024 01; 14(1):1093. doi: 10.1038/s41598-024-51625-3. [PMID: 38212440]
  • Shugao Fan, Xiao Xu, Jianmin Chen, Yanling Yin, Ying Zhao. Genome-wide identification, characterization, and expression analysis of m6A readers-YTH domain-containing genes in alfalfa. BMC genomics. 2024 Jan; 25(1):18. doi: 10.1186/s12864-023-09926-w. [PMID: 38166738]
  • Xiurong Yang, Shuangyong Yan, Guangsheng Li, Yuejiao Li, Junling Li, Zhongqiu Cui, Shuqin Sun, Jianfei Huo, Yue Sun. Rice-Magnaporthe oryzae interactions in resistant and susceptible rice cultivars under panicle blast infection based on defense-related enzyme activities and metabolomics. PloS one. 2024; 19(3):e0299999. doi: 10.1371/journal.pone.0299999. [PMID: 38451992]
  • Peter Lüth, Henry Sila Nzioki, Claire Sands Baker, David Chandler Sands. A microbial bioherbicide for Striga hermonthica control: production, development, and effectiveness of a seed coating agent. Pest management science. 2024 Jan; 80(1):149-155. doi: 10.1002/ps.7522. [PMID: 37139834]
  • Zeyu Wang, Yanchao Yang, Sirui Li, Weihua Ma, Kui Wang, Mario Soberón, Shuo Yan, Jie Shen, Frederic Francis, Alejandra Bravo, Jie Zhang. JAK/STAT signaling regulated intestinal regeneration defends insect pests against pore-forming toxins produced by Bacillus thuringiensis. PLoS pathogens. 2024 Jan; 20(1):e1011823. doi: 10.1371/journal.ppat.1011823. [PMID: 38236820]
  • Wen-Yu Peng, Bizunesh Abere, Haibin Shi, Sabrina Toland, Thomas E Smithgall, Patrick S Moore, Yuan Chang. Membrane-bound Merkel cell polyomavirus middle T protein constitutively activates PLCγ1 signaling through Src-family kinases. Proceedings of the National Academy of Sciences of the United States of America. 2023 Dec; 120(51):e2316467120. doi: 10.1073/pnas.2316467120. [PMID: 38079542]
  • Jinxia Wu, Zhenchang Li, Hongwei Zhu, Yajie Chang, Quanquan Li, Jing Chen, Guiping Shen, Jianghua Feng. Childhood overweight and obesity: age stratification contributes to the differences in metabolic characteristics. Obesity (Silver Spring, Md.). 2023 Dec; ?(?):. doi: 10.1002/oby.23964. [PMID: 38112246]
  • Martiniano Maria Ricardi, Niklas Wallmeroth, Cecilia Cermesoni, Dietmar Gerald Mehlhorn, Sandra Richter, Lei Zhang, Josephine Mittendorf, Ingeborg Godehardt, Kenneth Wayne Berendzen, Edda von Roepenack-Lahaye, York-Dieter Stierhof, Volker Lipka, Gerd Jürgens, Christopher Grefen. A tyrosine phospho-switch within the Longin domain of VAMP721 modulates SNARE functionality. The Plant journal : for cell and molecular biology. 2023 Dec; 116(6):1633-1651. doi: 10.1111/tpj.16451. [PMID: 37659090]
  • Jin Su, Youqing Dong, Xinran Yu, Limin Zhang, Wen Li. Exploring the mechanism of action of total glucosides of paeony against autoimmune thyroiditis based on network pharmacology and molecular docking. Medicine. 2023 Dec; 102(48):e36290. doi: 10.1097/md.0000000000036290. [PMID: 38050229]
  • Jorge El-Azaz, Bethany Moore, Yuri Takeda-Kimura, Ryo Yokoyama, Micha Wijesingha Ahchige, Xuan Chen, Matthew Schneider, Hiroshi A Maeda. Coordinated regulation of the entry and exit steps of aromatic amino acid biosynthesis supports the dual lignin pathway in grasses. Nature communications. 2023 11; 14(1):7242. doi: 10.1038/s41467-023-42587-7. [PMID: 37945591]
  • Huitong Zhou, Wenhao Li, Lingrong Bai, Jiqing Wang, Yuzhu Luo, Shaobin Li, Jonathan G H Hickford. Ovine KRTAP36-2: A New Keratin-Associated Protein Gene Related to Variation in Wool Yield. Genes. 2023 Nov; 14(11):. doi: 10.3390/genes14112045. [PMID: 38002988]
  • Ke Yi, Huimin Kong, Chunxiong Zheng, Chenya Zhuo, Yuanyuan Jin, Qingguo Zhong, Rachel L Mintz, Enguo Ju, Haixia Wang, Shixian Lv, Yeh-Hsing Lao, Yu Tao, Mingqiang Li. A LIGHTFUL nanomedicine overcomes EGFR-mediated drug resistance for enhanced tyrosine-kinase-inhibitor-based hepatocellular carcinoma therapy. Biomaterials. 2023 11; 302(?):122349. doi: 10.1016/j.biomaterials.2023.122349. [PMID: 37844429]
  • Shuai Dong, Long Wang, Huiting Qin, Hongbin Zhan, Donghao Wang, Xiaoyan Cao. Expression Patterns and Functional Analysis of Three SmTAT Genes Encoding Tyrosine Aminotransferases in Salvia miltiorrhiza. International journal of molecular sciences. 2023 Oct; 24(21):. doi: 10.3390/ijms242115575. [PMID: 37958559]
  • Mykhailo Girych, Waldemar Kulig, Giray Enkavi, Ilpo Vattulainen. How Neuromembrane Lipids Modulate Membrane Proteins: Insights from G-Protein-Coupled Receptors (GPCRs) and Receptor Tyrosine Kinases (RTKs). Cold Spring Harbor perspectives in biology. 2023 10; 15(10):. doi: 10.1101/cshperspect.a041419. [PMID: 37487628]
  • Sen Qiao, Tianwei Wang, Hongmei Wang. Dysregulated ceramides metabolism via PTPN11 exposes a metabolic vulnerability to breast cancer metastasis. Medical oncology (Northwood, London, England). 2023 Sep; 40(11):310. doi: 10.1007/s12032-023-02187-3. [PMID: 37773553]
  • Jacinta L Watkins, Qiushi Li, Sam Yeaman, Peter J Facchini. Elucidation of the mescaline biosynthetic pathway in peyote (Lophophora williamsii). The Plant journal : for cell and molecular biology. 2023 Sep; ?(?):. doi: 10.1111/tpj.16447. [PMID: 37675639]
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